Publications

Examples of results obtained with instrumentation at NeCEN can be found in publications below.

2024

• Kros, A. et al. Structure–function relationship of phase-separated liposomes containing diacylglycerol analogues. Biomaterial Science, 2024. https://doi.org/10.1039/D4BM00799A
• Borowska, A.M., Chiariello, M.G., Garaeva, A.A. et al. Structural basis of the obligatory exchange mode of human neutral amino acid transporter ASCT2. Nat Commun 15, 6570 (2024). https://doi.org/10.1038/s41467-024-50888-8
• Llerena Schiffmacher, D.A., Lee, SH., Kliza, K.W. et al. The small CRL4^CSA ubiquitin ligase component DDA1 regulates transcription-coupled repair dynamics. Nat Commun 15, 6374 (2024). https://doi.org/10.1038/s41467-024-50584-7
• Van Os, W.L. et al. Lipid conjugate dissociation analysis improves the in vivo understanding of lipid-based nanomedicine. Journal of Controlled Release, 2024. https://doi.org/10.1016/j.jconrel.2024.05.034
• Gogou, C., Beugelink, J.W., Frias, C.P. et al. Alternative splicing controls teneurin-3 compact dimer formation for neuronal recognition. Nat Comm., 2024. https://doi.org/10.1038/s41467-024-47763-x
• Koornneef, A., Vanshylla, K., Hardenberg, G. et al., CoPoP liposomes displaying stabilized clade C HIV-1 Env elicit tier 2 multiclade neutralization in rabbits. Nat Comm., 2024. https://doi.org/10.1038/s41467-024-47492-1
• Podoliak, E., Lamm, G.H.U., Marin, E. et al, A subgroup of light-driven sodium pumps with an additional Schiff base counterion. Nat. Comm., 2024. https://doi.org/10.1038/s41467-024-47469-0
• Dsouza, L. et al., An integrated approach towards extracting structural characteristics of chlorosomes from a bchQ mutant of Chlorobaculum tepidum. Phys Chem Chem Phys. 2024 10.1039/d4cp00221k
• Pattipeiluhu, R., Zeng, Y., Hendrix, M.M. et al., Liquid crystalline inverted lipid phases encapsulating siRNA enhance lipid nanoparticle mediated transfection. Nat. Comm., 2024. 10.1038/s41467-024-45666-5

2023

• Ongenae, V., Kempff, A., van Neer, V. et al., Genome sequence and characterization of Streptomyces phages Vanseggelen and Verabelle, representing two new species within the genus Camvirus. Sci Rep 13, 2023. https://doi.org/10.1038/s41598-023-47634-3
• Bos, R. et al., Biophysical studies do not reveal direct interactions between human PF4 and Ad26.COV2.S vaccine. Journal of Thrombosis and Haemostasis, 2023. https://doi.org/10.1016/j.jtha.2023.12.020
• Kalienkova, V. et al., Structures of a sperm-specific solute carrier gated by voltage and cAMP. Nature, 2023. https://doi.org/10.1038/s41586-023-06629-w 
• Botto, M., et al., A four-point molecular handover during Okazaki maturation. Nature Structural and Molecular Biology, 2023. https://doi.org/10.1038/s41594-023-01071-y 
• Zhang, Y., et al., Charging of Vitreous Samples in Cryogenic Electron Microscopy Mitigated by Graphene. ACS, 2023. https://doi.org/10.1021/acsnano.3c03722
• Thangaratnarajah, C. et al., Expulsion mechanism of the substrate-translocating subunit in ECF transporters. Nat. Commun. 14, 2023. https://doi.org/10.1038/s41467-023-40266-1
• Muok, A.R. et al., A new class of protein sensor links spirochete pleomorphism, persistence, and chemotaxis. nBio, 2023. https://doi.org/10.1101/2022.01.11.475842 
• Han, X. et al., CryoEM analysis of the essential native UDP-glucose pyrophosphorylase from Aspergillus nidulans reveals key conformations for activity regulation and function. mBio, 2023. https://doi.org/10.1128/mbio.00414-23
• Leung, M. et al., Structural specializations of the sperm tail. Cell, 2023. https://doi.org/10.1016/j.cell.2023.05.026
• Colucci, E. et al., Mutation in glutamate transporter homologue GltTk provides insights into pathologic mechanism of episodic ataxia 6. Nat. Commun 14, 2023. https://doi.org/10.1038/s41467-023-37503-y
• Fermin, R. et al., The unusual distribution of spin-triplet supercurrents in disk-shaped Josephson junctions. ArXiv, 2023. https://doi.org/10.48550/arXiv.2303.07993
• Bak, J. et al., Extracting Modified Microtubules from Mammalian Cells to Study Microtubule-Protein Complexes by Cryo-Electron Microscopy. JoVE Journal, 2023.
• Du, W. et al., Avidity engineering of human heavy-chain-only antibodies mitigates neutralization resistance of SARS-CoV-2 variants. Frontiers in Immunology, 2023. https://doi.org/10.3389/fimmu.2023.1111385
• Papadopoulou, P. et al., Phase-separated Lipid-based nanoparticles: selective behavior at the nano-bio interface. Advanced Materials, 2023. https://doi.org/10.1002/adma.202310872
• Huber, S. et al., Cryo-EM structure of gas vesicles for buoyancy-controlled motility. Cell, 2023. https://doi.org/10.1016/j.cell.2023.01.041
• Sixma, T. et al., Unexpected moves: a conformational change in MutSα enables high-affinity DNA mismatch binding. Nucleic Acids Res. 2023. DOI: 10.1126/sciadv.add367 

2022

• Landskron L. et al., Posttranslational modification of microtubules by the MATCAP detyrosinase. Science, 2022. 10.1126/science.abn6020

• Ouyang, R., et al., High-resolution reconstruction of a Jumbo-bacteriophage infecting capsulated bacteria using hyperbranched tail fibers. Nature Communications, 2022. https://doi.org/10.1038/s41467-022-34972-5
• Gros, P. & El Mazouni, D. Cryo-EM structures of peripherin-2 an ROM1 suggest multiple roles in photoreceptor membrane morphogenesis. Science Advances, 2022. DOI: 10.1126/sciadv.add3677
• Fermin, R. et al., Mesoscopic superconducting memory based on bistable magnetic textures. Physical Review Research, 2022. 10.1103/PhysRevResearch.4.033136
• Ongenae, V. et al., Genome sequence and characterization of Streptomyces phage Pablito, representing a new species within the genus Janusvirus. Scientific Reports, 2022. https://doi.org/10.1038/s41598-022-22784-y
• Ongenae, V. et al., Reversible bacteriophage resistance by shedding the bacterial cell wall. Open Biology, 2022. 10.1098/rsob.210379
• Depelteau, J., et al., UVC inactivation of pathogenic samples suitable for cryo-EM analysis. Commun. Biology, 2022. 10.1038/s42003-021-02962-w
• Xie, Y. et al., Two types of liposomal formulations improve the therapeutic ratio of prednisolone phosphate in a zebrafish model for inflammation. Cells, 2022. 10.3390/cells11040671
• Meijer, D.H. et al., Teneurin4 dimer structures reveak a calcium-stabilized compact conformation supporting homomeric trans-interactions. The EMBO Journal, 2022. doi.org/10.15252/embj.2020107505
• Borsellini, A. et al., Cryogenic electron microscopy structures reveal how ATP and DNA binding in MutS coordinates sequential steps of DNA mismatch repair. Nature Structural & Molecular Biology, 2022. https://www.nature.com/articles/s41594-021-00707-1
• Hurdiss, D.L. et al., Fluoxetine targets on allosteric site in the entovirus 2C AAA+ ATPase and stabilizes a ring-shaped hexameric complex. Science advances, 2022. 10.1126/sciadv.abj7615
• Semchonok, D.A. et al., Cryo-EM structure of a tetrameric photosystem I from Chroococcidiopsis TS-821, a thermophilic, unicellular, non-heterocyst-forming cyanobacterium. Plant Commun., 2022. 10.1016/j.xplc.2021.100248
• Fermin, R. et al., Superconducting triplet rim currents in a spin-textured ferromagnetic disk. Nano Lett., 2022. 10.1021/acs.nanolett.1c04051
• Borsellini, A. et al., MutL binds to 3' resected DNA ends and blocks DNA polymerase access. Nucleic Acid Research, 2022. 

2021

• Rheinberger, J. et al., Optimized cryo-EM data-acquisition workflow by sample thickness determination. Acta Crystallographica D, 2021. https://doi.org/10.1107/S205979832100334X
• Gambelli, L. et al., The polygonal cell shape and surface protein layer of anaerobic mathane-oxidizing Methylomirabilis Ianthanidiphila bacteria. Front Microbiology, 2021. 10.3389/fmicb.2021.766527
• Muok, A. et al., Microbial hitchhiking: how Streptomyces spores are transported by motile soil bacteria. ISME Journal, 2021. 10.1038/s41396-021-00952-8
• Leung, M.R. et al., Membrane remodeling and matrix dispersal intermediates during mammalian arosomal exocytosis. Front Cell Dev. Biology, 2021 10.3389/fcell.2021.765673
• Leung, M.R. et al., In-cell structyres of conserved supramolecular protein arrays at the mitochondria-cytoskeleton interface in mammalian sperm. PNAS, 2021. 10.1073/pnas.2110996118
• Leung, M.R. et al., The multi-scale architecture of mammalian sperm flagella and implications for ciliary motility. EMBO Journal, 2021 10.15252/embj.2020107410
• Noone, D.P. et al., Cryo-electron microscopy and biochemical analysis offer Insights into the effects of acidic pH, such as occur during acidosis, on the complement binding properties of C-reactive protein. Front Immunology, 2021 0.3389/fimmu.2021.757633

• Gijsbers, A. et al., Mycobacterium tuberculosis ferritin: a suitable workhorse protein for cryo-EM development. Acta Crystallographica D, 2021 10.1107/S2059798321007233
• Gijsbers, A. et al., Priming mycobacterial ESX-secreted protein B to form a channel-like structure. Current Research in Structural Biology, 2021 10.1016/j.crstbi.2021.06.001
• Kaplan, M., Chreifi, G., Metskas, L.A., Liedtke, J. et al. In situ imaging of bacterial outer membrane projections and associated protein complexes using electron cryo-tomography. eLife 2021;10:e73099 doi.org/10.7554/eLife.73099
• Juraszek, J., Rutten, L., Blokland, S. et al. Stabilizing the closed SARS-CoV-2 spike trimer. Nature Communications 12, 244 (2021). doi.org/10.1038/s41467-020-20321-x

2020

• Zhou, X.Q. et al., The self-assembly of a cyclometalated palladium photosensitizer into protein-stabilized nanords triggers drug uptake in vitro and in vivo. J. Am. Chem. Soc., 2020. 10.1021/jacs.0c01369
• Arias-Alpizar, G. et al., Light-triggered switching of liposome surface charge directs delivery of membrane impermeable payloads in vivo. Nat. Commun., 2020. 10.1038/s41467-020-17360-9
• Muok, A.R., Ortega, D.R., Kurniyati, K. et al. Atypical chemoreceptor arrays accommodate high membrane curvature. Nat Commun 11, 5763 (2020). doi.org/10.1038/s41467-020-19628-6
• Muok, A.R. et al. & Briegel A., Engineered chemotaxis core signaling units indicate a constrained kinase-off state. Science Signaling 13, issue 657, 2020. doi.org/10.1126/scisignal.abc1328
• Justen, A.M. et al. & Briegel A., Polysaccharide length affects mycobacterial cell shape and antibiotic susceptibility. Science Advances 6, no. 38, 2020. doi.org/10.1126/sciadv.aba4015
• Bąk, K.M. et al., Light-triggered switching of liposome surface charge directs delivery of membrane impermeable payloads in vivo. Nat Commun 11, 3638 (2020). doi.org/10.1038/s41467-020-17360-9
• Bąk, K.M. et al., Oxyanion transport across lipid bilayers: direct measurements in large and giant unilamellar vesicles. Chem. Commun., 2020, 56, 4910-4913 doi.org/10.1039/C9CC09888G
• Zhao, X et al., The Self-Assembly of a Cyclometalated Palladium Photosensitizer into Protein-Stabilized Nanorods Triggers Drug Uptake In Vitro and In Vivo. J. Am. Chem. Soc. 2020, 142, 23, 10383–10399 doi.org/10.1021/jacs.0c01369
• Wolff G. et al. & Barcena M. , A molecular pore spans the double membrane of the coronavirus replication organelle. Science doi.org/10.1126/science.abd3629
• Ultee, E. et al. & Briegel A., Teichoic acids anchor distinct cell wall lamellae in an apically growing bacterium. Commun Biol doi.org/10.1038/s42003-020-1038-6

2019

• Wolff G, et al. & Barcena M, Mind the gap: Micro-expansion joints drastically decrease the bending of FIB-milled cryo-lamellae. JSB doi.org/10.1016/j.jsb.2019.09.006
• Andres G, Charro D, et al. & Abrescia NGA, The cryo-EM structure of African swine fever virus unravels a unique architecture comprising two icosahedral protein capsids and two lipoprotein membranes. JBC doi.org/10.1074/jbc.AC119.011196
• Leidreiter F, Roderer D, et al. & Raunser S, Common architecture of Tc toxins from human and insect pathogenic bacteria. Science Advances doi.org/10.1126/sciadv.aax6497

• Halfon Y, et al. & Yonath A, Structure of Pseudomonas aeruginosa ribosomes from an aminoglycoside-resistant clinical isolate. PNAS doi.org/10.1073/pnas.1909831116 (iNEXT financial support)

• Famelis N, Rivera-Cazalda A, et al. Llorca O & Geibel S, Architecture of the mycobacterial type VII secretion system. Nature doi.org/10.1038/s41586-019-1633-1

• Wilson MD, Renault L, et al. & Costa A, Retroviral integration into nucleosomes through DNA looping and sliding along the histone octamer. Nat. Comm. doi.org/10.1038/s41467-019-12007-w

• Cerofolini L, et al. & Calderone V, Integrative approaches in structural biology: a more complete picture from the combination of individual techniques. Biomolecules doi.org/10.3390/biom9080370

• Yang W, et al. & Briegel A, In Situ Conformational Changes of the Escherichia coli Serine Chemoreceptor in Different Signaling States. mBio Asm doi.org/10.1128/mBio.00973-19

• Sun Z, et al. & de Groot H, A Semisynthetic Peptide−Metalloporphyrin Responsive Matrix for Artificial Photosynthesis. ChemPhotoChem doi.org/10.1002/cptc.201900063

• Sharp TH, et al. & Gros P, Insights into IgM-mediated complement activation based on in situ structures of IgM-C1-C4b. PNAS doi.org/10.1073/pnas.1901841116

• Ivic N, et al. & Halic M, Fuzzy Interactions Form and Shape the Histone Transport Complex. Mol. Cell. doi.org/10.1016/j.molcel.2019.01.032 (Instruct-ERIC financial support)

• Brenzinger S, et al. & Briegel A, Structural and Proteomic Changes in Viable but Non-culturable Vibrio cholerae. Front. Microbiol. doi.org/10.3389/fmicb.2019.00793 (Instruct-ERIC financial support)

• Ferreira JL, et al. & Beeby M, γ-proteobacteria eject their polar flagella under nutrient depletion, retaining flagellar motor relic structures. PLOS Biology doi.org/10.1371/journal.pbio.3000165

• Santos-Perez I, et al. & Abrescia NGA, Structural basis for assembly of vertical single β-barrel viruses. Nature Communications doi.org/10.1038/s41467-019-08927-2

2018

• Willegems K & Efremov RG, Influence of lipids mimetics on gating of ryanodine receptor. Structure doi.org/10.1016/j.str.2018.06.010

• Yang W, et al. & Briegel A, Baseplate variability of Vibrio choleraechemoreceptor arrays. PNAS doi.org/10.1073/pnas.1811931115

• Cai S, et al. & Gan L, Cryo-ET reveals the macromolecular reorganization of S. pombe mitotic chromosomes in vivo. PNAS doi.org/10.1073/pnas.1720476115

• Gatsogiannis C, et al. & Raunser S, Tc toxin activation requires unfolding and refolding of a β-propeller. Nature doi: 10.1038/s41586-018-0556-6

• Thomas B, et al. & de Groot HJM, A Molecular Level Approach To Elucidate the Supramolecular Packing of Light‐Harvesting Antenna Systems. Chemistry doi: 10.1002/chem.201802288

• Stanishneva-Konovalova TB, et al. & Kurochkina LP, Cryo-EM Structure of the Single-Ring Chaperonin from Bacteriophage OBP P. fluorescence. Microscopy and Microanalysis doi:10.1017/S1431927618006700 

• Jackson VA, et al., & Seiradake E, Structures of teneurin adhesion receptors reveal an ancient fold for cell-cell interaction. Nature Communications doi: 10.1038/s41467-018-03460-0

• Garcia-Nafria J, et al. & Tate CG, Cryo-EM structure of the serotonin 5-HT1B receptor coupled to heterotrimeric Go. Nature doi: 10.1038/s41586-018-0241-9

• Ugurlar D, et al. & Gros P, Structures of C1-IgG1 provide insights into how danger pattern recognition activates complement. Science doi:10.1126/science.aao4988

2017

• Abid Ali F, et al. & Costa A, Cryo-EM Structure of a Licensed DNA Replication Origin. Nature Commmunications doi:10.1038/s41467-017-02389-0
• Bhat JY, et al. & Wendler P & Hayer-Hartl M, Mechanism of Enzyme Repair by the AAA+ chaperone rubisco activase. Mol. Cell. doi:10.1016/j.molcel.2017.07.004 (iNEXT financial support)
• Mosalaganti S, et al. & Musacchio A, Structure of the RZZ Complex and Molecular Basis of its Interaction with Spindly. Journal of Cell Biology doi:10.1083/jcb.201611060
• Hesketh EL, et al. & Ranson NA, The Structures of a Naturally Empty Cowpea Mosaic Virus Particle and its Genome-Containing Counterpart by Cryo-Electron Microscopy. Scientific Reports doi:10.1038/s41598-017-00533-w
• Clabbers MTB, et al. & Abrahams JP, Protein Structure Determination by Electron Diffraction Using a Single Three-Dimensional Nanocrystal. Acta Crystallographica Section D Biological Crystallography doi:10.1107/S2059798317010348
• Thomas B, et al. & de Groot HJM, Determination of Controlled Self-Assembly of a Paracrystalline Material by Homology Modelling with Hybrid NMR and TEM. Chemistry doi:10.1002/chem.201701172
• Sundaramoorthy R, et al. & Owen-Hughes T, Structural Reorganization of the Chromatin Remodeling Enzyme Chd1 Upon Engagement with Nucleosomes. eLIFE doi:10.7554/eLife.22510
• Franken LE, et al. & Guskov A, A General Mechanism of Ribosome Dimerization Revealed by Single-Particle Cryo-Electron Microscopy. Nature Communications doi:10.1038/s41467-017-00718-x
• Bilokapic A, Strauss M & Halic M, Histone Octamer rearranges to adapt to DNA Unwrapping. Nature Communications doi:10.1038/s41594-017-0005-5 (Instruct-ERIC support)
• Arenz S, et al. & Wilson DN, A Combined Cryo-EM and Molecular Dynamics Approach Reveals the Mechanism of ErmBL-mediated Translation Arrest. Nature Communications doi:1038/ncomms12026

• Zamora M, et al. & Valle M, Potyvirus Virion Structure Shows Conserved Protein Fold and RNA Binding Site in ssRNA Viruses. Science Advances doi:10.1126/sciadv.aao2182

• Haglin ER, et al. & Thompson LK, His-Tag Mediated Dimerization of Chemoreceptors Leads to Assembly of Functional Nanoarrays. Biochemistry doi:10.1021/acs.biochem.7b00698

• Afanasyev P, et al. & van Heel M, Single-Particle Cryo-EM Alignment by Classification (ABC): The Structure of Lumbricus terrestris Haemoglobin. IUCrJ doi:10.1107/S2052252517010922

• Alewijnse B, et al. & Potter CS, Best Practices for Managing Large CryoEM Facilities. Journal of Structural Biology doi:10.1016/j.jsb.2017.07.011

• Van Bezouwen L, et al. Boekema EJ, Subunit and Chlorophyll Organization of the Plant Photosystem II Supercomplex. Nature Plants doi:10.1038/nplants.2017.80

• Thomas B, et al. & de Groot HJM, A Hybrid Solid State NMR and Electron Microscopy Structure Determination Protocol for Engineering Advanced Para-crystalline Optical Materials. Chemistry  doi:10.1002/chem.201700324

2016

• Iacovache I, et al., Cryo-EM Structure of Aerolysin Variants Reveals a Novel Protein Fold and the Pore-Formation Process. Nature Communications doi:10.1038/ncomms12062

• Arenz S, et al., A Combined Cryo-EM and Molecular Dynamics Approach Reveals the Mechanism of ErmBL-Mediated Translation Arrest. Nature Communications doi:10.1038/ncomms12026 

• Sobti M, et al., Cryo-EM Structures of the Autoinhibited E. coli ATP Synthase in Three Rotational States. eLIFE doi:10.7554/eLife.21598

• Coureux PD, et al., Cryo-EM Study of Start Codon Selection During Archaeal Translation Initiation. Nature Communications doi:10.1038/ncomms13366

• Sharp TH, et al., Imaging Complement by Phase-Plate Cryo-Electron Tomography from Initiation to Pore Formation. Journal of Structural Biology doi:10.1016/j.jsb.2016.09.008

• Vazquez-Fernandez E, et al., The Structural Architecture of an Infectious Mammalian Prion using Electron Cryomicroscopy. PLOS Pathogens doi:10.1371/journal.ppat.1005835

• Van Heel M, et al., Multivariate Statistical Analysis of Large Datasets: Single Particle Electron Microscopy.  Open Journal of Statistics doi:10.4236/ojs.2016.64059

• Iacovache I, et al., Cryo-EM Structure of Aerolysin Variants Reveals a novel Protein Fold and the Pore-Formation Process. Nature Communications doi:10.1038/ncomms12062

• Larburu N, et al., Structure of a Human Pre-40S Particle Points to a Role for RACK1 in the Final Steps of 18S rRNA Processing. Nucleic Acids Research doi:10.1093/nar/gkw714

• Shishovs M, et al., Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages. Journal of Molecular Biology doi:10.1016/j.jmb.2016.08.025 

• Koning R, et al., Asymmetric Cryo-EM Reconstruction of Phage MS2 Reveals Genome Structure in situ. Nature Communications doi:10.1038/ncomms12524

• Stuart D, et al., The Democratization of Cryo-EM. Nature Methods doi:10.1038/nmeth.3946

• Shakeel S, et al., Multiple Capsid-Stabilizing Interactions Revealed in a High-Resolution Structure of an Emerging Picornavirus Causing Neonatal Sepsis. Nature Communications doi:10.1038/ncomms11387

• Von der Ecken J, et al., Cryo-EM Structure of a Human Cytoplasmic Actomyosin Complex at Near-Atomic Resolution. Nature doi:10.1038/nature18295

• Celler K, et al., Cross-Membranes Orchestrate Compartmentalization and Morphogenesis in Streptomyces. Nature Communications doi:10.1038/ncomms11836

• Arenz S, et al., Structures of the Orthosomycin Antibiotics Avilamycin and Evernimicin in Complex with the Bacterial 70S Ribosome. PNAS doi:10.1073/pnas.1604790113

• Yewdall NA, et al., Structures of Human Peroxiredoxin 3 Suggest Self-Chaperoning Assembly that Maintains Catalytic State. Structure doi:10.1016/j.str.2016.04.013

• Sharp TH, et al., Heterogeneous MAC Initiator and Pore Structures in a Lipid Bilayer by Phase-Plate Cryo-electron Tomography. Cell Reports doi:10.1016/j.celrep.2016.03.002

2015

• Beckert B, et al., Translational Arrest by a Prokaryotic Signal Recognition Particle is Mediated by RNA Interactions. Nature Structural and Molecular Biology doi:10.1038/nsmb.3086

• Diebolder CA, et al., Cryoelectron Tomography of the NAIP5/NLRC4 Inflammasome: Implications for NLR Activation. Structure doi:10.1016/j.str.2015.10.001

• Efremov RG, et al., Architecture and Conformational Switch Mechanism of the Ryanodine Receptor. Nature doi:10.1038/nature13916

• Von der Ecken J, et al., Structure of the F-Actin-Tropomyosin Complex. Nature doi:10.1038/nature14033

• Afanasyev P, et al., A posteriori Correction of Camera Characteristics from Large Image Data Sets. Scientific Reports doi:10.1038/srep10317

• Maskell DP, et al., Structural Basis for Retroviral Integration into Nucleosomes. Nature doi:10.1038/nature14495

• Sohmen D, et al., Structure of the Bacillus subtilis 70S Ribosome Reveals the Basis for Species-Specific Stalling. Nature Communications doi:10.1038/ncomms7941

• Arenz S, et al., Cryo-EM Structure of the Tetracycline Resistance Protein TetM in Complex with a Translating Ribosome at 3.9Å Resolution. PNAS doi:10.1073/pnas.1501775112

2014

• Voortman LM, et al., Quantifying Resolution Limiting Factors in Subtomogram Averaged Cryo-Electron Tomography Using Simulations. Journal of Structural Biology doi:10.1016/j.jsb.2014.06.007

• Diebolder CA, et al., Complement is Activated by IgG Hexamers Assembled at the Cell Surface. Science doi:10.1126/science.1248943

• Bischoff L, et al., Molecular Basis for the Ribosome Functioning as an L-Tryptophan Sensor. Cell Reports doi:10.1016/j.celrep.2014.09.011

• Arenz S, et al., Drug Sensing by the Ribosome Induces Translational Arrest via Active Site Perturbation. Molecular Cell doi:10.1016/j.molcel.2014.09.014

2013

• Nederlof I, et al., Imaging Protein Three-Dimensional Nanocrystals with Cryo-EM. Acta Crystallographica Section D Biological Crystallography doi:10.1107/S0907444913002734

• Vulovic M, et al., Image Formation Modeling in Cryo-Electron Microscopy. Journal of Structural Biology doi:10.1016/j.jsb.2013.05.008